ID   Y3793_MYCBO             Reviewed;         314 AA.
AC   Q7TVQ7; A0A1R3Y563; X2BPS7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb3793c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BQ2027_MB3793C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU02422.1; -; Genomic_DNA.
DR   RefSeq; NP_857430.1; NC_002945.3.
DR   RefSeq; WP_003420557.1; NC_002945.4.
DR   AlphaFoldDB; Q7TVQ7; -.
DR   SMR; Q7TVQ7; -.
DR   EnsemblBacteria; SIU02422; SIU02422; BQ2027_MB3793C.
DR   PATRIC; fig|233413.5.peg.4149; -.
DR   OMA; DSMPPTL; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..314
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase Mb3793c"
FT                   /id="PRO_0000361135"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34755 MW;  BACD884305460F6E CRC64;
     MPRTDNDSWA ITESVGATAL GVAAARAAET ESDNPLINDP FARIFVDAAG DGIWSMYTNR
     TLLAGATDLD PDLRAPIQQM IDFMAARTAF FDEYFLATAD AGVRQVVILA SGLDSRAWRL
     PWPDGTVVYE LDQPKVLEFK SATLRQHGAQ PASQLVNVPI DLRQDWPKAL QKAGFDPSKP
     CAWLAEGLVR YLPARAQDLL FERIDALSRP GSWLASNVPG AGFLDPERMR RQRADMRRMR
     AAAAKLVETE ISDVDDLWYA EQRTAVAEWL RERGWDVSTA TLPELLARYG RSIPHSGEDS
     IPPNLFVSAQ RATS